Rapid conversion of angiotensin I to angiotensin II by neutrophil and mast cell proteinases.
Human neutrophil cathepsin G and human skin mast cell chymase rapidly convert angiotensin I to angiotensin II with only minor cleavage elsewhere in the molecule. The rate of cleavage is consistent with a potential role for either or both of these enzymes in an alternate pathway for angiotensin II synthesis. Since neither enzyme in inhibited by captopril, an angiotensin converting enzyme inactivator, it is possible that leukocyte and mast cell enzymes may play a significant role in the development of abnormally high local concentrations of angiotensin II, associated with various inflammatory processes.
D000596:Amino Acids / Q000032:analysis; D000803:Angiotensin I / Q000378:metabolism*; D000804:Angiotensin II / Q000378:metabolism*; D000809:Angiotensins / Q000378:metabolism*; D002216:Captopril / Q000494:pharmacology; D056649:Cathepsin G; D002403:Cathepsins / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D012085:Chymosin / Q000378:metabolism*; D006801:Humans; D008407:Mast Cells / Q000201:enzymology*; D009504:Neutrophils / Q000201:enzymology*; D012697:Serine Endopeptidases; D012867:Skin / Q000201:enzymology; D013997:Time Factors
D000596:Amino Acids; D000809:Angiotensins; D000804:Angiotensin II; D000803:Angiotensin I; D002216:Captopril; D002403:Cathepsins; D012697:Serine Endopeptidases; C534094:CTSG protein, human; D056649:Cathepsin G; D012085:Chymosin